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Separation of soybean leghemoglobin components by isoelectric focusing in immobilized pH gradients
Author(s) -
Puppo Alain,
Rigaud Jean
Publication year - 1987
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150080408
Subject(s) - leghemoglobin , isoelectric focusing , chemistry , chromatography , resolution (logic) , nitrogen fixation , hemeprotein , isoelectric point , nitrogen , heme , biochemistry , enzyme , organic chemistry , computer science , root nodule , artificial intelligence
Soybean leghemoglobin subcomponents were separated with good resolution in immobilized pH gradients, both at the analytical and preparative scales. In the latter case, the tedious step of gel washing could be omitted without affecting resolution. This procedure appeared as the only one suitable for preparing large amounts of highly purified leghemoglobin c 1 , c 2 and c 3 , allowing their further characterization and an investigation of their specific roles in nitrogen fixation.